BRENDA - Enzyme Database
show all sequences of 2.6.1.39

2-Aminoadipate-2-oxoglutarate aminotransferase isoenzymes in human liver: a plausible physiological role in lysine and tryptophan metabolism

Okuno, E.; Tsujimoto, M.; Nakamura, M.; Kido, R.; Enzyme Protein 47, 136-148 (1993)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.25
-
2-Aminoadipate
pH 8.0, 37°C isoenzyme AadAT-II
Homo sapiens
1
-
2-oxoadipate
pH 8.0, 37°C isoenzyme AadAT-II
Homo sapiens
1.1
-
2-oxoglutarate
pH 8.0, 37°C isoenzyme AadAT-I
Homo sapiens
1.4
-
glutamate
pH 8.0, 37°C
Homo sapiens
2.5
-
2-oxoadipate
pH 8.0, 37°C isoenzyme AadAT-I
Homo sapiens
3.2
-
2-oxoglutarate
pH 8.0, 37°C isoenzyme AadAT-II
Homo sapiens
12.5
-
L-glutamate
pH 8.0, 37°C, isoenzyme AadAT-II
Homo sapiens
20
-
2-Aminoadipate
pH 8.0, 37°C
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
isoenzyme AadAT-I
Homo sapiens
5737
-
cytosol
-
Homo sapiens
5829
-
mitochondrion
isoenzyme AadAT-II
Homo sapiens
5739
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
46000
-
2 * 46000, SDS-PAGE
Homo sapiens
98000
-
isoenzyme AadAT-II, sucrose density gradient centrifugation
Homo sapiens
104000
-
isoenzyme AadAT-I, sucrose density gradient centrifugation
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-2-aminoadipate + 2-oxoglutarate
Homo sapiens
lysine and tryptophan metabolism
2-oxoadipate + L-glutamate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
human
-
Purification (Commentary)
Commentary
Organism
2 isoenzymes, AadAT-I and AadAT-II
Homo sapiens
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Homo sapiens
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.77
-
isoenzyme AadAT-I
Homo sapiens
10.68
-
isoenzyme AadAT-II
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
kynurenine + 2-oxoglutarate
-
639983
Homo sapiens
kynurenic acid + L-glutamate
-
-
-
ir
L-2-aminoadipate + 2-oxoglutarate
-
639983
Homo sapiens
2-oxoadipate + L-glutamate
-
639983
Homo sapiens
r
L-2-aminoadipate + 2-oxoglutarate
lysine and tryptophan metabolism
639983
Homo sapiens
2-oxoadipate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
-
639983
Homo sapiens
3-indole-2-oxopropanoate + L-glutamate
-
-
-
?
additional information
2 isoenzymes, AadAT-I and AadAT-II, isoenzyme AadAT-II shows additional activity with tryptophan or kynurenine-2-oxoglutarate reaction, only slight activity with asparagine, alanine, arginine, ornithine, isoleucine, valine, leucine, lysine, serine, threonine, phenylalanine, tyrosine, histidine, glutamine, methionine or aspartate with 2-oxoglutarate
639983
Homo sapiens
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 * 46000, SDS-PAGE
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
9.5
isoenzyme AadAT-II
Homo sapiens
9.5
-
isoenzyme AadAT-I
Homo sapiens
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
9
9.5
isoenzyme AadAT-I, sensitive to pH changes, activity is quickly lost at a higher pH, isoenzyme AadAT-II is less sensitive to pH changes
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.25
-
2-Aminoadipate
pH 8.0, 37°C isoenzyme AadAT-II
Homo sapiens
1
-
2-oxoadipate
pH 8.0, 37°C isoenzyme AadAT-II
Homo sapiens
1.1
-
2-oxoglutarate
pH 8.0, 37°C isoenzyme AadAT-I
Homo sapiens
1.4
-
glutamate
pH 8.0, 37°C
Homo sapiens
2.5
-
2-oxoadipate
pH 8.0, 37°C isoenzyme AadAT-I
Homo sapiens
3.2
-
2-oxoglutarate
pH 8.0, 37°C isoenzyme AadAT-II
Homo sapiens
12.5
-
L-glutamate
pH 8.0, 37°C, isoenzyme AadAT-II
Homo sapiens
20
-
2-Aminoadipate
pH 8.0, 37°C
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
isoenzyme AadAT-I
Homo sapiens
5737
-
cytosol
-
Homo sapiens
5829
-
mitochondrion
isoenzyme AadAT-II
Homo sapiens
5739
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
46000
-
2 * 46000, SDS-PAGE
Homo sapiens
98000
-
isoenzyme AadAT-II, sucrose density gradient centrifugation
Homo sapiens
104000
-
isoenzyme AadAT-I, sucrose density gradient centrifugation
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-2-aminoadipate + 2-oxoglutarate
Homo sapiens
lysine and tryptophan metabolism
2-oxoadipate + L-glutamate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
2 isoenzymes, AadAT-I and AadAT-II
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Homo sapiens
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.77
-
isoenzyme AadAT-I
Homo sapiens
10.68
-
isoenzyme AadAT-II
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
kynurenine + 2-oxoglutarate
-
639983
Homo sapiens
kynurenic acid + L-glutamate
-
-
-
ir
L-2-aminoadipate + 2-oxoglutarate
-
639983
Homo sapiens
2-oxoadipate + L-glutamate
-
639983
Homo sapiens
r
L-2-aminoadipate + 2-oxoglutarate
lysine and tryptophan metabolism
639983
Homo sapiens
2-oxoadipate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
-
639983
Homo sapiens
3-indole-2-oxopropanoate + L-glutamate
-
-
-
?
additional information
2 isoenzymes, AadAT-I and AadAT-II, isoenzyme AadAT-II shows additional activity with tryptophan or kynurenine-2-oxoglutarate reaction, only slight activity with asparagine, alanine, arginine, ornithine, isoleucine, valine, leucine, lysine, serine, threonine, phenylalanine, tyrosine, histidine, glutamine, methionine or aspartate with 2-oxoglutarate
639983
Homo sapiens
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 46000, SDS-PAGE
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
9.5
isoenzyme AadAT-II
Homo sapiens
9.5
-
isoenzyme AadAT-I
Homo sapiens
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
9
9.5
isoenzyme AadAT-I, sensitive to pH changes, activity is quickly lost at a higher pH, isoenzyme AadAT-II is less sensitive to pH changes
Homo sapiens
Other publictions for EC 2.6.1.39
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
737334
Rzad
Characterization of two aminot ...
Candida albicans, Candida albicans ATCC MYA-2876
Acta Biochim. Pol.
62
903-912
2015
-
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1
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-
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-
2
-
-
4
-
-
2
-
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-
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3
1
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-
1
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1
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2
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4
-
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3
1
-
-
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-
1
-
-
-
-
-
-
-
-
-
739600
Bulfer
Crystal structure of Saccharom ...
Saccharomyces cerevisiae
Protein Sci.
22
1417-1424
2013
-
-
1
1
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
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1
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1
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721430
Karsten
Mechanism of the aromatic amin ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
516
67-74
2011
-
-
1
-
-
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-
6
-
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1
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1
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1
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5
1
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4
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1
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1
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1
1
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6
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1
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1
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5
1
-
-
-
4
-
1
-
-
-
-
-
-
-
-
703133
Han
Structure, expression, and fun ...
Homo sapiens, Mus musculus, Rattus norvegicus
Cell. Mol. Life Sci.
67
353-368
2010
-
-
-
1
-
-
1
-
1
-
-
-
-
3
-
-
1
-
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4
-
-
1
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3
-
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1
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1
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1
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1
-
4
-
-
1
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
721926
Han
Thermal stability, pH dependen ...
Mus musculus
BMC Biochem.
11
0019
2010
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
1
-
-
1
-
1
-
1
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1
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1
-
1
-
1
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
702069
Ouchi
Dual roles of a conserved pair ...
Thermus thermophilus
Biochem. Biophys. Res. Commun.
388
21-27
2009
-
-
1
1
3
-
-
24
-
-
-
-
-
2
-
-
1
-
-
-
-
-
4
-
-
-
-
12
-
-
-
1
-
-
-
-
-
1
1
1
3
-
-
-
-
24
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
12
-
-
-
-
-
-
-
-
24
24
689965
Tomita
Mechanism for multiple-substra ...
Thermus thermophilus
Proteins
75
348-359
2008
-
-
-
1
-
-
-
-
-
-
-
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2
-
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5
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1
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1
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5
-
-
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1
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-
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-
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-
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-
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-
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702779
Han
Substrate specificity and stru ...
Homo sapiens
Biosci. Rep.
28
205-215
2008
-
-
-
-
-
-
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-
1
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2
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1
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1
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1
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659885
Miyazaki
alpha-Aminoadipate aminotransf ...
Thermus thermophilus
Microbiology
150
2327-2334
2004
-
-
1
-
1
-
-
4
-
-
3
-
-
4
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7
-
7
1
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4
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1
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1
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4
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3
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7
-
7
1
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-
-
4
-
-
-
-
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-
-
-
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639985
Goh
Characterization of the human ...
Homo sapiens
Mol. Genet. Metab.
76
172-180
2002
-
1
1
-
-
-
-
-
-
-
1
1
-
7
-
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-
8
-
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2
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1
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1
2
1
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1
1
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8
-
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2
-
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-
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-
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-
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636625
Buchli
Cloning and functional express ...
Rattus norvegicus
J. Biol. Chem.
270
29330-29335
1995
-
1
1
-
-
-
-
-
-
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3
1
-
2
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1
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1
1
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4
1
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1
1
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3
1
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1
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1
1
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4
1
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-
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-
-
-
-
-
-
-
-
-
639983
Okuno
2-Aminoadipate-2-oxoglutarate ...
Homo sapiens
Enzyme Protein
47
136-148
1993
-
-
-
-
-
-
-
8
3
-
3
1
-
2
-
-
1
-
-
3
2
-
5
1
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
3
-
3
1
-
-
-
1
-
3
2
-
5
1
-
-
-
-
2
-
1
-
-
-
-
-
-
-
636621
Mawal
-
Purification and properties of ...
Rattus norvegicus
Biochem. J.
279
595-599
1991
-
-
-
-
-
-
-
-
-
-
-
1
-
1
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1
-
-
1
-
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3
-
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1
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1
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1
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3
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
636622
Mawal
alpha-Aminoadipate and kynuren ...
Rattus norvegicus
J. Biol. Chem.
266
2573-2575
1991
-
-
-
-
-
-
-
-
1
-
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-
-
3
-
-
1
-
-
3
-
-
1
-
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-
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-
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-
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1
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1
-
3
-
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
639981
Mawal
Purification and properties of ...
Rattus norvegicus
Prep. Biochem.
21
63-73
1991
-
-
-
-
-
-
-
-
-
-
2
-
-
2
-
-
1
-
-
2
-
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1
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2
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1
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2
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1
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-
-
-
-
639979
Deshmukh
Purification and properties of ...
Bos taurus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Biochem. J.
261
761-768
1989
-
-
-
-
-
1
19
4
4
-
2
2
-
165
-
-
2
-
-
4
1
2
26
2
-
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-
2
-
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2
-
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-
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-
2
-
-
1
-
19
-
4
4
-
2
2
-
-
-
2
-
4
1
2
26
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
636620
Hartline
Kynurenine aminotransferase fr ...
Rattus norvegicus
Methods Enzymol.
113
664-672
1985
-
-
-
-
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